title: Purification and some properties of the hemolytic toxin aerolysin.
abstract: Aerolysin, the hemolytic toxin produced by Aeromonas hydrophila, has been purified by a combination of salt fractionation, gel filtration, and ion-exchange and hydroxyapatite chromatography. The resulting protein has a molecular weight of 51 500 and appears homogeneous by polyacrylamide gel electrophoresis in sodium dodecyl sulphate. It is free of detectable protease and phospholipase activities. The purified protein can be separated into two active components with pIs of 5.39 and 5.46 by isoelectric focusing. Both components are found in the original culture supernatant indicating that the multiplicity is not due to proteolysis during isolation. Purified aerolysin is unstable even at 25 degrees C and its hemolytic action is inhibited by certain reducing agents including ferrous iron and cysteine. It appears to be the only toxin hemolytic to human cells that is produced by A. hydrophila under the conditions described.
mesh_terms: D000333:Aeromonas; D001427:Bacterial Toxins / Q000302:isolation & purification*; D002413:Cations, Divalent / Q000494:pharmacology; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D004492:Edetic Acid / Q000494:pharmacology; D004591:Electrophoresis, Polyacrylamide Gel; D006460:Hemolysin Proteins / Q000494:pharmacology*; D006801:Humans; D007525:Isoelectric Focusing; D008970:Molecular Weight; D052899:Pore Forming Cytotoxic Proteins
chemical_list: D001427:Bacterial Toxins; D002413:Cations, Divalent; D006460:Hemolysin Proteins; D052899:Pore Forming Cytotoxic Proteins; C032676:aerolysin; D004492:Edetic Acid